about
CbpA acts as a modulator of HspR repressor DNA binding activity in Helicobacter pyloriStructure of CbpA J-domain bound to the regulatory protein Cbpm explains its specificity and suggests evolutionary link between Cbpm and transcriptional regulators.DNA recognition by Escherichia coli CbpA protein requires a conserved arginine-minor-groove interactionComplex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM.The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.Proteolysis in the Escherichia coli heat shock response: a player at many levels.Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes.Conserved central domains control the quaternary structure of type I and type II Hsp40 molecular chaperones.Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA.
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P2860
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@ast
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@en
type
label
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@ast
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@en
prefLabel
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@ast
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@en
P2093
P2860
P356
P1476
In vivo modulation of a DnaJ homolog, CbpA, by CbpM.
@en
P2093
Matthew R Chenoweth
Nancy Trun
Sue Wickner
P2860
P304
P356
10.1128/JB.01757-06
P407
P577
2007-03-02T00:00:00Z